8R57
CryoEM structure of wheat 40S ribosomal subunit, head domain
Summary for 8R57
Entry DOI | 10.2210/pdb8r57/pdb |
EMDB information | 18903 |
Descriptor | Plectin/eS10 N-terminal domain-containing protein, Small ribosomal subunit protein uS14, Ribosomal protein RACK1 subfamily. WD repeat G protein beta family, ... (20 entities in total) |
Functional Keywords | small ribosomal subunit, wheat, eukaryotes, 40s, ribosome |
Biological source | Triticum aestivum (bread wheat) More |
Total number of polymer chains | 16 |
Total formula weight | 848230.42 |
Authors | Kravchenko, O.V.,Baymukhametov, T.N.,Afonina, Z.A.,Vasilenko, K.S. (deposition date: 2023-11-16, release date: 2023-12-27, Last modification date: 2024-04-24) |
Primary citation | Kravchenko, O.V.,Baymukhametov, T.N.,Afonina, Z.A.,Vassilenko, K.S. High-Resolution Structure and Internal Mobility of a Plant 40S Ribosomal Subunit. Int J Mol Sci, 24:-, 2023 Cited by PubMed Abstract: Ribosome is a major part of the protein synthesis machinery, and analysis of its structure is of paramount importance. However, the structure of ribosomes from only a limited number of organisms has been resolved to date; it especially concerns plant ribosomes and ribosomal subunits. Here, we report a high-resolution cryo-electron microscopy reconstruction of the small subunit of the (common wheat) cytoplasmic ribosome. A detailed atomic model was built that includes the majority of the rRNA and some of the protein modifications. The analysis of the obtained data revealed structural peculiarities of the 40S subunit in the monocot plant ribosome. We applied the 3D Flexible Refinement approach to analyze the internal mobility of the 40S subunit and succeeded in decomposing it into four major motions, describing rotations of the head domain and a shift in the massive rRNA expansion segment. It was shown that these motions are almost uncorrelated and that the 40S subunit is flexible enough to spontaneously adopt any conformation it takes as a part of a translating ribosome or ribosomal complex. Here, we introduce the first high-resolution structure of an isolated plant 40S subunit and the first quantitative analysis of the flexibility of small ribosomal subunits, hoping that it will help in studying various aspects of ribosome functioning. PubMed: 38139282DOI: 10.3390/ijms242417453 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.55 Å) |
Structure validation
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